期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 19, 期 1, 页码 84-U105出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2202
关键词
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资金
- Eidgenossische Technische Hochschule (ETH)
- Swiss National Science Foundation [CRSII3_127454]
- Krebsforschung Schweiz (KFS) [02648-08-2010]
- SNF [205321_124720]
Lin28 inhibits the biogenesis of let-7 miRNAs through a direct interaction with the terminal loop of pre-let-7. This interaction requires the zinc-knuckle domains of Lin28. We show that the zinc knuckle domains of Lin28 are sufficient to provide binding selectivity for pre-let-7 miRNAs and present the NMR structure of human Lin28 zinc knuckles bound to the short sequence 5'-AGGAGAU-3'. The structure reveals that each zinc knuckle recognizes an AG dinucleotide separated by a single nucleotide spacer. This defines a new 5'-NGNNG-3' consensus motif that explains how Lin28 selectively recognizes pre-let-7 family members. Binding assays in cell lysates and functional assays in cultured cells demonstrate that the interactions observed in the solution structure also occur between the full-length protein and members of the pre-let-7 family. The consensus sequence explains several seemingly disparate previously published observations on the binding properties of Lin28.
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